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A model of the complex between human beta-microseminoprotein and CRISP-3 based on NMR data.

Ghasriani, Houman LU ; Fernlund, Per LU ; Udby, Lene and Drakenberg, Torbjörn LU (2009) In Biochemical and Biophysical Research Communications 378(2). p.235-239
Abstract
beta-Microseminoprotein (MSP), a 10kDa seminal plasma protein, forms a tight complex with cysteine-rich secretory protein 3 (CRISP-3) from granulocytes. The 3D structure of human MSP has been determined but there is as yet no 3D structure for CRISP-3. We have now studied the complex between human MSP and CRISP-3 with multidimensional NMR. (15)N-HSQC spectra show substantial differences between free and complexed hMSP. Using several 3D-NMR spectra of triply labeled hMSP in complex with a recombinant N-terminal domain of CRISP-3, most of the backbone of hMSP could be assigned. The data show that only one side of hMSP, comprising beta-strands 1, 4, 5, and 8 are affected by the complex formation, indicating that beta-strands 1 and 8 form the... (More)
beta-Microseminoprotein (MSP), a 10kDa seminal plasma protein, forms a tight complex with cysteine-rich secretory protein 3 (CRISP-3) from granulocytes. The 3D structure of human MSP has been determined but there is as yet no 3D structure for CRISP-3. We have now studied the complex between human MSP and CRISP-3 with multidimensional NMR. (15)N-HSQC spectra show substantial differences between free and complexed hMSP. Using several 3D-NMR spectra of triply labeled hMSP in complex with a recombinant N-terminal domain of CRISP-3, most of the backbone of hMSP could be assigned. The data show that only one side of hMSP, comprising beta-strands 1, 4, 5, and 8 are affected by the complex formation, indicating that beta-strands 1 and 8 form the main binding surface. Based on this we present a tentative structure for the hMSP-CRISP-3 complex using the known crystal structure of triflin as a model of CRISP-3. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical and Biophysical Research Communications
volume
378
issue
2
pages
235 - 239
publisher
Elsevier
external identifiers
  • wos:000262063100018
  • pmid:19026612
  • scopus:57049165364
ISSN
1090-2104
DOI
10.1016/j.bbrc.2008.11.040
language
English
LU publication?
yes
id
2c7ef51c-74c5-494b-a717-16bc0e810cb0 (old id 1271181)
date added to LUP
2009-02-10 16:10:12
date last changed
2017-01-01 06:06:55
@article{2c7ef51c-74c5-494b-a717-16bc0e810cb0,
  abstract     = {beta-Microseminoprotein (MSP), a 10kDa seminal plasma protein, forms a tight complex with cysteine-rich secretory protein 3 (CRISP-3) from granulocytes. The 3D structure of human MSP has been determined but there is as yet no 3D structure for CRISP-3. We have now studied the complex between human MSP and CRISP-3 with multidimensional NMR. (15)N-HSQC spectra show substantial differences between free and complexed hMSP. Using several 3D-NMR spectra of triply labeled hMSP in complex with a recombinant N-terminal domain of CRISP-3, most of the backbone of hMSP could be assigned. The data show that only one side of hMSP, comprising beta-strands 1, 4, 5, and 8 are affected by the complex formation, indicating that beta-strands 1 and 8 form the main binding surface. Based on this we present a tentative structure for the hMSP-CRISP-3 complex using the known crystal structure of triflin as a model of CRISP-3.},
  author       = {Ghasriani, Houman and Fernlund, Per and Udby, Lene and Drakenberg, Torbjörn},
  issn         = {1090-2104},
  language     = {eng},
  number       = {2},
  pages        = {235--239},
  publisher    = {Elsevier},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {A model of the complex between human beta-microseminoprotein and CRISP-3 based on NMR data.},
  url          = {http://dx.doi.org/10.1016/j.bbrc.2008.11.040},
  volume       = {378},
  year         = {2009},
}